메뉴 건너뛰기




Volumn 16, Issue 12, 1996, Pages 7063-7071

Role of the mitochondrial DnaJ homolog Mdj1p as a chaperone for mitochondrially synthesized and imported proteins

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; MITOCHONDRIAL DNA; POLYPEPTIDE; PROTEIN PRECURSOR;

EID: 0029860683     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.12.7063     Document Type: Article
Times cited : (69)

References (73)
  • 1
    • 0024978377 scopus 로고
    • Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage λ DNA replication
    • Alfano, C., and R. McMacken. 1989. Heat shock protein-mediated disassembly of nucleoprotein structures is required for the initiation of bacteriophage λ DNA replication. J. Biol. Chem. 254:10709-10718.
    • (1989) J. Biol. Chem. , vol.254 , pp. 10709-10718
    • Alfano, C.1    McMacken, R.2
  • 2
    • 85035180916 scopus 로고    scopus 로고
    • Bio-Rad Laboratories, Richmond, Calif.
    • Bio-Rad Laboratories. Muta-Gene manual. Bio-Rad Laboratories, Richmond, Calif.
    • Muta-Gene Manual
  • 3
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5′-phosphatc decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J. D., F. LaCroute, and G. R. Fink. 1984. A positive selection for mutants lacking orotidine-5′-phosphatc decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet. 197:345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    LaCroute, F.2    Fink, G.R.3
  • 5
    • 0027759380 scopus 로고
    • A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome
    • Brodsky, J. L., and R. Schekman. 1993. A Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposome. J. Cell Biol. 123:1355-1363.
    • (1993) J. Cell Biol. , vol.123 , pp. 1355-1363
    • Brodsky, J.L.1    Schekman, R.2
  • 8
    • 0027300506 scopus 로고
    • Heat shock proteins: Molecular chaperones of protein biogenesis
    • Craig, E. A., B. D. Gambill, and R. J. Nelson. 1993. Heat shock proteins: molecular chaperones of protein biogenesis. Microbiol. Rev. 57:402-414.
    • (1993) Microbiol. Rev. , vol.57 , pp. 402-414
    • Craig, E.A.1    Gambill, B.D.2    Nelson, R.J.3
  • 9
    • 0028353336 scopus 로고
    • DnaJ-like proteins: Molecular chaperones and specific regulators of Hsp70
    • Cyr, D. M., T. Langer, and M. G. Douglas. 1994. DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70. Trends Biochem. Sci. 19:176-181.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 176-181
    • Cyr, D.M.1    Langer, T.2    Douglas, M.G.3
  • 10
    • 0022515029 scopus 로고
    • Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria
    • London
    • Eilers, M., and G. Schatz. 1986. Binding of a specific ligand inhibits import of a purified precursor protein into mitochondria. Nature (London) 322: 228-232.
    • (1986) Nature , vol.322 , pp. 228-232
    • Eilers, M.1    Schatz, G.2
  • 12
    • 0028361309 scopus 로고
    • Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones
    • London
    • Frydman, J., E. Nimmesgern, K. Ohtsuka, and F.-U. Hartl. 1994. Folding of nascent polypeptide chains in a high molecular mass assembly with molecular chaperones. Nature (London) 370:111-117.
    • (1994) Nature , vol.370 , pp. 111-117
    • Frydman, J.1    Nimmesgern, E.2    Ohtsuka, K.3    Hartl, F.-U.4
  • 15
    • 0026733631 scopus 로고
    • The emergence of the chaperone machines
    • Georgopoulos, C. 1992. The emergence of the chaperone machines. Trends Biochem. Sci. 17:295-299.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 295-299
    • Georgopoulos, C.1
  • 16
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St. Jean, R. A. Woods, and R. H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 17
    • 0004330520 scopus 로고
    • Guide to yeast genetics and molecular biology. Academic Press, Inc., San Diego, Calif.
    • Guthrie, C., and G. R. Fink (ed.). 1991. Methods in enzymology, vol. 194. Guide to yeast genetics and molecular biology. Academic Press, Inc., San Diego, Calif.
    • (1991) Methods in Enzymology , vol.194
    • Guthrie, C.1    Fink, G.R.2
  • 18
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 19
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick, J. P., and F.-U. Hartl. 1995. The role of molecular chaperones in protein folding. FASEB J. 9:1559-1569.
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 20
    • 0027425585 scopus 로고
    • Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides
    • Hendrick, J. P., T. Langer, T. Davis, F.-U. Hartl, and M. Wiedmann. 1993. Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc. Natl. Acad. Sci. USA 90:10216-10220.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10216-10220
    • Hendrick, J.P.1    Langer, T.2    Davis, T.3    Hartl, F.-U.4    Wiedmann, M.5
  • 21
    • 0000379406 scopus 로고
    • Isolation of yeast mitochondria and study of mitochondrial protein translation
    • In J. E. Celis (ed.), Academic Press, Inc., San Diego, Calif.
    • Herrmann, J. M., H. Fölsch, W. Neupert, and R. A. Stuart. 1994. Isolation of yeast mitochondria and study of mitochondrial protein translation, p. 538-544. In J. E. Celis (ed.), Cell biology: a laboratory manual. Academic Press, Inc., San Diego, Calif.
    • (1994) Cell Biology: A Laboratory Manual , pp. 538-544
    • Herrmann, J.M.1    Fölsch, H.2    Neupert, W.3    Stuart, R.A.4
  • 23
    • 0028073776 scopus 로고
    • Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA
    • Herrmann, J. M., R. A. Stuart, E. A. Craig, and W. Neupert. 1994. Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA. J. Cell Biol. 127:893-902.
    • (1994) J. Cell Biol. , vol.127 , pp. 893-902
    • Herrmann, J.M.1    Stuart, R.A.2    Craig, E.A.3    Neupert, W.4
  • 24
    • 0029913836 scopus 로고    scopus 로고
    • Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains
    • Hesterkamp, T., S. Hauser, H. Lütcke, and B. Bukau. 1996. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc. Natl. Acad. Sci. USA 93:4437-4441.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4437-4441
    • Hesterkamp, T.1    Hauser, S.2    Lütcke, H.3    Bukau, B.4
  • 25
    • 0029651968 scopus 로고
    • 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78)
    • 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78). Biochemistry 34:5587-5596.
    • (1995) Biochemistry , vol.34 , pp. 5587-5596
    • Hill, R.B.1    Flanagan, J.M.2    Prestegard, J.H.3
  • 26
    • 0028137887 scopus 로고
    • YGE1 is a yeast homolog of Escherichia coli grpE and is required for maintenance of mitochondrial functions
    • Ikeda, E., S. Yoshida, H. Mitsuzawa, I. Uno, and A. Toh-e. 1994. YGE1 is a yeast homolog of Escherichia coli grpE and is required for maintenance of mitochondrial functions. FEBS Lett. 339:265-268.
    • (1994) FEBS Lett. , vol.339 , pp. 265-268
    • Ikeda, E.1    Yoshida, S.2    Mitsuzawa, H.3    Uno, I.4    Toh-e, A.5
  • 27
    • 0025039149 scopus 로고
    • Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins
    • London
    • Kang, P. J., J. Ostermann, J. Shilling, W. Neupert, E. A. Craig, and N. Pfanner. 1990. Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins. Nature (London) 348:137-143.
    • (1990) Nature , vol.348 , pp. 137-143
    • Kang, P.J.1    Ostermann, J.2    Shilling, J.3    Neupert, W.4    Craig, E.A.5    Pfanner, N.6
  • 28
    • 0028556615 scopus 로고
    • Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane
    • Kronidou, N. G., W. Oppliger, L. Bolliger, K. Hannavy, B. S. Glick, G. Schatz, and M. Horst. 1994. Dynamic interaction between Isp45 and mitochondrial hsp70 in the protein import system of the yeast mitochondrial inner membrane. Proc. Natl. Acad. Sci. USA 91:12818-12822.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12818-12822
    • Kronidou, N.G.1    Oppliger, W.2    Bolliger, L.3    Hannavy, K.4    Glick, B.S.5    Schatz, G.6    Horst, M.7
  • 29
    • 0028850629 scopus 로고
    • Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins
    • Laloraya, S., P. J. T. Dekker, W. Voos, E. A. Craig, and N. Pfanner. 1995. Mitochondrial GrpE modulates the function of matrix Hsp70 in translocation and maturation of preproteins. Mol. Cell. Biol. 15:7098-7105.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 7098-7105
    • Laloraya, S.1    Dekker, P.J.T.2    Voos, W.3    Craig, E.A.4    Pfanner, N.5
  • 30
    • 0028356858 scopus 로고
    • A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation
    • Laloraya, S., B. D. Gambill, and E. A. Craig. 1994. A role for a eukaryotic GrpE-related protein, Mge1p, in protein translocation. Proc. Natl. Acad. Sci. USA 91:6481-6485.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6481-6485
    • Laloraya, S.1    Gambill, B.D.2    Craig, E.A.3
  • 31
    • 0026596223 scopus 로고
    • Successive action of molecular chaperones DnaK, DnaJ and GroEL along the pathway of assisted protein folding
    • London
    • Langer, T., C. Lu, H. Echols, J. Flanagan, M. K. Hayer, and F.-U. Hartl. 1992. Successive action of molecular chaperones DnaK, DnaJ and GroEL along the pathway of assisted protein folding. Nature (London) 356:683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.-U.6
  • 32
    • 0003081906 scopus 로고
    • Chaperoning mitochondrial biogenesis
    • R. I. Morimoto, A. Tessieres, and C. Georgopoulos (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Langer, T., and W. Neupert. 1994. Chaperoning mitochondrial biogenesis, p. 53-83. In R. I. Morimoto, A. Tessieres, and C. Georgopoulos (ed.), The biology of heat shock proteins and molecular chaperones. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1994) The Biology of Heat Shock Proteins and Molecular Chaperones , pp. 53-83
    • Langer, T.1    Neupert, W.2
  • 33
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., J. Marszalek, D. Ang, C. Georgopoulos, and M. Zylicz. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88:2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 34
    • 0026070260 scopus 로고
    • Sequential action of mitochondrial chaperones in protein import into the matrix
    • Manning-Krieg, U. C., P. E. Scherer, and G. Schatz. 1991. Sequential action of mitochondrial chaperones in protein import into the matrix. EMBO J. 10:3273-3280.
    • (1991) EMBO J. , vol.10 , pp. 3273-3280
    • Manning-Krieg, U.C.1    Scherer, P.E.2    Schatz, G.3
  • 35
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J. S., A. Buchberger, J. Reinstein, and B. Bukau. 1995. The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249:126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 36
    • 0027230956 scopus 로고
    • Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae
    • Nelson, M. K., T. Kurihara, and P. Silver. 1993. Extragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae. Genetics 134:159-173.
    • (1993) Genetics , vol.134 , pp. 159-173
    • Nelson, M.K.1    Kurihara, T.2    Silver, P.3
  • 37
    • 0025970971 scopus 로고
    • Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae
    • Nguyen, T. H., D. T. S. Law, and D. B. Williams. 1991. Binding protein BiP is required for translocation of secretory proteins into the endoplasmic reticulum in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 88:1565-1569.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1565-1569
    • Nguyen, T.H.1    Law, D.T.S.2    Williams, D.B.3
  • 38
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • London
    • Ostermann, J., A. L. Horwich, W. Neupert, and F.-U. Hartl. 1989. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature (London) 341:125-130.
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.-U.4
  • 40
    • 0030040712 scopus 로고    scopus 로고
    • Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation
    • Prip-Buus, C., B. Westermann, M. Schmitt, T. Langer, W. Neupert, and E. Schwarz. 1996. Role of the mitochondrial DnaJ homologue, Mdj1p, in the prevention of heat-induced protein aggregation. FEBS Lett. 380:142-146.
    • (1996) FEBS Lett. , vol.380 , pp. 142-146
    • Prip-Buus, C.1    Westermann, B.2    Schmitt, M.3    Langer, T.4    Neupert, W.5    Schwarz, E.6
  • 41
    • 0028046847 scopus 로고
    • Mitochondrial protein import: Biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44
    • Rassow, J., A. C. Maarse, E. Krainer, M. Kübrich, H. Müller, M. Meijer, E. A. Craig, and N. Pfanner. 1994. Mitochondrial protein import: biochemical and genetic evidence for interaction of matrix hsp70 and the inner membrane protein MIM44. J. Cell Biol. 127:1547-1556.
    • (1994) J. Cell Biol. , vol.127 , pp. 1547-1556
    • Rassow, J.1    Maarse, A.C.2    Krainer, E.3    Kübrich, M.4    Müller, H.5    Meijer, M.6    Craig, E.A.7    Pfanner, N.8
  • 42
    • 0030078788 scopus 로고    scopus 로고
    • Protein biogenesis: Chaperones for nascent polypeptides
    • Rassow, J., and N. Pfanner. 1996. Protein biogenesis: chaperones for nascent polypeptides. Curr. Biol. 6:115-118.
    • (1996) Curr. Biol. , vol.6 , pp. 115-118
    • Rassow, J.1    Pfanner, N.2
  • 44
    • 0024835142 scopus 로고
    • Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast
    • Rothblatt, J. A., R. J. Deshaies, S. L. Sanders, G. Daum, and R. Schekman. 1989. Multiple genes are required for proper insertion of secretory proteins into the endoplasmic reticulum in yeast. J. Cell Biol. 109:2641-2652.
    • (1989) J. Cell Biol. , vol.109 , pp. 2641-2652
    • Rothblatt, J.A.1    Deshaies, R.J.2    Sanders, S.L.3    Daum, G.4    Schekman, R.5
  • 45
    • 0028284879 scopus 로고
    • Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding
    • Rowley, N., C. Prip-Buus, B. Westermann, C. Brown, E. Schwarz, B. Barrell, and W. Neupert. 1994. Mdj1p, a novel chaperone of the DnaJ family, is involved in mitochondrial biogenesis and protein folding. Cell 77:249-259.
    • (1994) Cell , vol.77 , pp. 249-259
    • Rowley, N.1    Prip-Buus, C.2    Westermann, B.3    Brown, C.4    Schwarz, E.5    Barrell, B.6    Neupert, W.7
  • 47
    • 0029021905 scopus 로고
    • A yeast DnaJ homolog, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s
    • Schlenstedt, G., S. Harris, B. Risse, R. Lill, and P. Silver. 1995. A yeast DnaJ homolog, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s. J. Cell Biol. 129:979-988.
    • (1995) J. Cell Biol. , vol.129 , pp. 979-988
    • Schlenstedt, G.1    Harris, S.2    Risse, B.3    Lill, R.4    Silver, P.5
  • 48
    • 0022404366 scopus 로고
    • Transport of proteins into mitochondria: Translocation intermediates spanning contact sites between outer and inner membrane
    • Schleyer, M., and W. Neupert. 1985. Transport of proteins into mitochondria: translocation intermediates spanning contact sites between outer and inner membrane. Cell 43:339-350.
    • (1985) Cell , vol.43 , pp. 339-350
    • Schleyer, M.1    Neupert, W.2
  • 50
    • 0027427986 scopus 로고
    • DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., T. Langer, F.-U. Hartl, and B. Bukau. 1993. DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12:4137-1144.
    • (1993) EMBO J. , vol.12 , pp. 4137-11144
    • Schröder, H.1    Langer, T.2    Hartl, F.-U.3    Bukau, B.4
  • 51
    • 0027322148 scopus 로고
    • 2 into the mitochondrial intermembrane space: Specific recognition of the sorting signal
    • 2 into the mitochondrial intermembrane space: specific recognition of the sorting signal. EMBO J. 12:2295-2302.
    • (1993) EMBO J. , vol.12 , pp. 2295-2302
    • Schwarz, E.1    Seytter, T.2    Guiard, B.3    Neupert, W.4
  • 52
    • 0027136175 scopus 로고
    • Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologs of DnaK and DnaJ in the endoplasmic reticulum
    • Scidmore, M. A., H. H. Okamura, and M. D. Rose. 1993. Genetic interactions between KAR2 and SEC63, encoding eukaryotic homologs of DnaK and DnaJ in the endoplasmic reticulum. Mol. Biol. Cell 4:1145-1159.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1145-1159
    • Scidmore, M.A.1    Okamura, H.H.2    Rose, M.D.3
  • 53
    • 0024669291 scopus 로고
    • A system of shuttle vectors and host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 54
    • 0027169533 scopus 로고
    • Eukaryotic DnaJ homologs and the specificity of Hsp70 activity
    • Silver, P. A., and J. C. Way. 1993. Eukaryotic DnaJ homologs and the specificity of Hsp70 activity. Cell 74:5-6.
    • (1993) Cell , vol.74 , pp. 5-6
    • Silver, P.A.1    Way, J.C.2
  • 55
    • 0025931801 scopus 로고
    • Analysis of mitochondrial import using translocation intermediates and specific antibodies
    • Söllner, T., J. Rassow, and N. Pfanner. 1991. Analysis of mitochondrial import using translocation intermediates and specific antibodies. Methods Cell Biol. 34:345-358.
    • (1991) Methods Cell Biol. , vol.34 , pp. 345-358
    • Söllner, T.1    Rassow, J.2    Pfanner, N.3
  • 56
    • 0024226522 scopus 로고
    • Escherichia coli heat shock gene mutants are defective in proteolysis
    • Straus, D. B., W. A. Walter, and C. A. Gross. 1988. Escherichia coli heat shock gene mutants are defective in proteolysis. Genes Dev. 2:1851-1858.
    • (1988) Genes Dev. , vol.2 , pp. 1851-1858
    • Straus, D.B.1    Walter, W.A.2    Gross, C.A.3
  • 57
    • 0027958293 scopus 로고
    • Mitochondrial molecular chaperones: Their role in protein translocation
    • Stuart, R. A., D. M. Cyr, E. A. Craig, and W. Neupert. 1994. Mitochondrial molecular chaperones: their role in protein translocation. Trends Biochem. Sci. 19:87-92.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 87-92
    • Stuart, R.A.1    Cyr, D.M.2    Craig, E.A.3    Neupert, W.4
  • 58
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
    • Szabo, A., R. Korszun, F.-U. Hartl, and J. Flanagan. 1996. A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J. 15:408-417.
    • (1996) EMBO J. , vol.15 , pp. 408-417
    • Szabo, A.1    Korszun, R.2    Hartl, F.-U.3    Flanagan, J.4
  • 59
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE
    • Szabo, A., T. Langer, H. Schröder, J. Flanagan, B. Bukau, and F.-U. Hartl. 1994. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system - DnaK, DnaJ, and GrpE. Proc. Natl. Acad. Sci. USA 91: 10345-10349.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.-U.6
  • 60
    • 0027987996 scopus 로고
    • NMR structure determination of the Escherichia coli DnaJ chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J-domain
    • Szyperski, T., M. Pellecchia, D. Wall, C. Georgopoulos, and K. Wüthrich. 1994. NMR structure determination of the Escherichia coli DnaJ chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J-domain. Proc. Natl. Acad. Sci. USA 91:11343-11347.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11343-11347
    • Szyperski, T.1    Pellecchia, M.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 62
    • 0029670827 scopus 로고    scopus 로고
    • The Δψ- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria
    • Ungermann, C., B. Guiard, W. Neupert, and D. M. Cyr. 1996. The Δψ- and Hsp70/MIM44-dependent reaction cycle driving early steps of protein import into mitochondria. EMBO J. 15:735-744.
    • (1996) EMBO J. , vol.15 , pp. 735-744
    • Ungermann, C.1    Guiard, B.2    Neupert, W.3    Cyr, D.M.4
  • 63
    • 0028117097 scopus 로고
    • The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
    • Ungermann, C., W. Neupert, and D. M. Cyr. 1994. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria. Science 266:1250-1253.
    • (1994) Science , vol.266 , pp. 1250-1253
    • Ungermann, C.1    Neupert, W.2    Cyr, D.M.3
  • 64
    • 0025339295 scopus 로고
    • Loss of BiP/Grp78 function blocks translocation of secretory proteins in yeast
    • Vogel, J. P., L. M. Misra, and M. D. Rose. 1990. Loss of BiP/Grp78 function blocks translocation of secretory proteins in yeast. J. Cell Biol. 110:1885-1895.
    • (1990) J. Cell Biol. , vol.110 , pp. 1885-1895
    • Vogel, J.P.1    Misra, L.M.2    Rose, M.D.3
  • 65
    • 0027994692 scopus 로고
    • Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes
    • Voos, W., B. D. Gambill, S. Laloraya, D. Ang, E. A. Craig, and N. Pfanner. 1994. Mitochondrial GrpE is present in a complex with hsp70 and preproteins in transit across membranes. Mol. Cell. Biol. 14:6627-6634.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6627-6634
    • Voos, W.1    Gambill, B.D.2    Laloraya, S.3    Ang, D.4    Craig, E.A.5    Pfanner, N.6
  • 66
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner, I., H. Arlt, L. van Dyck, T. Langer, and W. Neupert. 1994. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J. 13:5135-5145.
    • (1994) EMBO J. , vol.13 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    Van Dyck, L.3    Langer, T.4    Neupert, W.5
  • 67
    • 0028170215 scopus 로고
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication. J. Biol. Chem. 269:5446-5451.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 68
    • 0028930540 scopus 로고
    • The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone
    • Wall, D., M. Zylicz, and C. Georgopoulos. 1995. The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone. J. Biol. Chem. 270:2139-2144.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2139-2144
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 69
    • 0029020451 scopus 로고
    • The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria
    • Westermann, B., C. Prip-Buus, W. Neupert, and E. Schwarz. 1995. The role of the GrpE homologue, Mge1p, in mediating protein import and protein folding in mitochondria. EMBO J. 14:3452-3460.
    • (1995) EMBO J. , vol.14 , pp. 3452-3460
    • Westermann, B.1    Prip-Buus, C.2    Neupert, W.3    Schwarz, E.4
  • 70
    • 0025875276 scopus 로고
    • Functions of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA
    • London
    • Wickner, S., J. Hoskins, and K. McKenney. 1991. Functions of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA. Nature (London) 350:165-167.
    • (1991) Nature , vol.350 , pp. 165-167
    • Wickner, S.1    Hoskins, J.2    McKenney, K.3
  • 71
    • 0027994841 scopus 로고
    • How ATP drives proteins across membranes
    • Wickner, W. T. 1994. How ATP drives proteins across membranes. Science 266:1197-1198.
    • (1994) Science , vol.266 , pp. 1197-1198
    • Wickner, W.T.1
  • 72
    • 0026644011 scopus 로고
    • DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli
    • Wild, J., E. Altman, T. Yura, and C. A. Gross. 1992. DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli. Genes Dev. 6:1165-1172.
    • (1992) Genes Dev. , vol.6 , pp. 1165-1172
    • Wild, J.1    Altman, E.2    Yura, T.3    Gross, C.A.4
  • 73
    • 0024316732 scopus 로고
    • Initiation of λ DNA replication with purified host- And bacteriophage-encoded proteins: The role of the dnaK, dnaJ and grpE heat shock proteins
    • Zylicz, M., D. Ang, K. Liberek, and C. Georgopoulos. 1989. Initiation of λ DNA replication with purified host- and bacteriophage-encoded proteins: the role of the dnaK, dnaJ and grpE heat shock proteins. EMBO J. 8:1601-1608.
    • (1989) EMBO J. , vol.8 , pp. 1601-1608
    • Zylicz, M.1    Ang, D.2    Liberek, K.3    Georgopoulos, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.